ID   Y122_AZOSB              Reviewed;         347 AA.
AC   A1K1N5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Probable RNA methyltransferase azo0122;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=azo0122;
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72;
RX   PubMed=17057704; DOI=10.1038/nbt1243;
RA   Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA   Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA   Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA   Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT   "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT   strain BH72.";
RL   Nat. Biotechnol. 24:1385-1391(2006).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAL92740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM406670; CAL92740.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041642161.1; NC_008702.1.
DR   AlphaFoldDB; A1K1N5; -.
DR   SMR; A1K1N5; -.
DR   STRING; 62928.azo0122; -.
DR   EnsemblBacteria; CAL92740; CAL92740; azo0122.
DR   KEGG; azo:azo0122; -.
DR   eggNOG; COG0820; Bacteria.
DR   HOGENOM; CLU_029101_3_3_4; -.
DR   OrthoDB; 1111428at2; -.
DR   Proteomes; UP000002588; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040072; Methyltransferase_A.
DR   InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30544; PTHR30544; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF006004; CHP00048; 1.
DR   SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Disulfide bond; Iron; Iron-sulfur; Metal-binding;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..347
FT                   /note="Probable RNA methyltransferase azo0122"
FT                   /id="PRO_0000350020"
FT   DOMAIN          92..318
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        323
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   DISULFID        99..323
FT                   /note="(transient)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  38216 MW;  5C3499FDED7355D6 CRC64;
     MRIDDLTQRL RALGAKPAHE QRVLRAWVQR SSMDNRRQAA KDFLPLALRE ALPALTAELE
     GLARLRSQHP GEDGSARLLV ELADGQTVES VLLLRDGLCV STQLGCAVGC VFCMTGREGL
     LRQLGSAEIV AQVVLARSLR PVKKVVFMGM GEPAHNLDNV LEAIDLLGTA GGIGHKNLVF
     STVGDYRVFE RLPRQRVKPA LALSLHTTRA DLRAQLLPRA PQIAPQELVE LGERYARSTG
     YPIQYQWTLI EGVNDSPEEM DGIVRLLRGK YALMNLIPYN SVPELEFRRP GREAAVALAA
     YLHRHGVLAK LRQSAGQDVE GGCGQLRARV VKMDRRPRTA RATPPTA